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Insulin Activates Ras in the PC12 Cell Line

Title
Insulin Activates Ras in the PC12 Cell Line
Authors
Hwang J.-J.Kwon J.-H.Hur K.C.
Ewha Authors
허규정
SCOPUS Author ID
허규정scopus
Issue Date
1997
Journal Title
Molecules and Cells
ISSN
1016-8478JCR Link
Citation
vol. 7, no. 3, pp. 438 - 443
Indexed
SCI; SCIE; SCOPUS; KCI scopus
Abstract
To address whether Ras can be activated by insulin in the PC12 cell line, proteins interacting with insulin receptor and IRS-1 molecules and their tyrosine phosphorylation were analyzed by immunoblotting following immunoprecipitation with antibodies. Tyrosine phosphorylation of the insulin receptor and IRS-1 was increased by insulin. Grb2 and Ras-GAP appeared in the immunoprecipitates by anti-insulin receptor and anti-IRS-1 from insulin-treated cells. In addition, PI 3-kinase was activated by insulin treatment in this cell line and Grb2, Ras-GAP, and MAP kinase were coprecipitated with Ras from both insulin-treated and NGF-treated cells. Analysis of MAP kinases from insulin-treated cells revealed that insulin, like NGF, increased tyrosine phosphorylation. However, activation of the MAP kinase by NGF lasted longer than activation by insulin. These results indicate that Ras can be activated by insulin in the PC12 cell line and that Ras activation is neither an accurate nor a plausible method of discriminating signals between proliferation and differentiation.
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일반대학원 > 바이오융합과학과 > Journal papers
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